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Biomedical subjects

H Bazin

Publications and source records attributed to H Bazin.

At least 325 records · Page 18Linked to original sources
PubMed1975

Lymphocyte plasma membranes. III. Composition of lymphocyte plasma membranes from normal and immunized rats.

Isolated plasma membranes of thymic and splenic lymphocytes from unimmunized and immunized rats of the inbred ACI and F344 strains were analyzed for chemical and enzymatic composition, for membrane protein patterns by polyacrylamide gel electrophoresis and for membrane-associated immunoglobulins. After immunization, the thymic and splenic lymphocyte membranes from F344 rat contained less carbohydrate and higher phospholipid contents than control animals. In both ACI and F344 inbred rat strains the membrane phospholipid to cholesterol weight ratio increased significantly after immunization. The electrophoretic patterns of solubilized membrane proteins and of iodinated external membrane proteins were similar in unimmunized and immunized animals. When thymic and splenic lymphocytes of normal or immunized animals were surface radioidinated, solubilized in Triton X-100, NP-40 or 10 M urea in 1.5 M acetic acid and analyzed by immunoprecipitation, labeled IgM immunoglobulin was recovered from thymic lymphocytes but both labeled IgG and IgM were recovered from splenic lymphocytes. However, when unlabeled isolated plasma membranes were solubilized in 1 percent Triton X-100 and analyzed by immunodiffusion in agarose gels both IgG and IgM were identified in thymic and splenic cells.

Animals↗
PubMed1975

Half-lives of two types of rat homocytotropic antibodies in circulation and in the skin.

The half-lives of two classes of rat immunoglobulins with homocytotropic properties, i.e., IgE and IgG2a, in the circulating blood and in the skin were studied. The catabolism of both normal (reaginic) and pathological (myeloma) IgE proteins in circulation was found to be extremely rapid with a half-life of 12 h. In contrast, the half-life of IgE antibody in the homologous skin was calculated to be 7.4 days. On the other hand, the half-life of IgG2a in circulation was about 5 days regardless of normal or pathological origin. IgG2a protein was, however, rapidly cleared from the injected skin site with a half life of 2.4 days, a value not longer than that obtained with nonskin-sensitizing goat IgG. The results indicate that rat IgE has an extremely short half-life in circulation despite of its sensitization period in tissues, and that the affinity for the target cells, as well as the mode of sensitization, of the two classes of homocytotropic antibodies, IgE and IgG2a, is different.

Animals↗
PubMed1975

Identification and some properties of rat secretory component.

An antiserum, prepared against partially reduced and alkylated rat milk SIgA, was shown to contain antibodies reacting with a rat milk protein of alpha-2 mobility, which possessed antigenic determinants common with SIaA, eluted from Sephadex G-200 at the same position as mammalian secretory components, and could be released from rat SIgA by mild reduction and alkylation. This protein, called rat secretory component, was also detected in saliva, tears and urine. Rat free secretory component (FSC) possessed antigenic determinants which were inaccessible in rat SIgA, as found in other species. In vitro, ra FSC combined with rat serum polymeric IgA or IgM, but not with monomeric IgA or IgG. These data emphasize the many similarities between the human and rat SIgA systems.

Adsorption↗
PubMed1975

Transplantable immunoglobulin-secreting tumors in rats. VI. N-terminal sequence variability in LOU/C/Wsl rat monoclonal heavy chains.

Most of the spontaneous ileocecal immunocytomas of LOU/C/Wsl strain rats secrete large amounts of monoclonal immunoglobulins. Amino acid sequence studies were undertaken on the heavy chains of 13 of these proteins and on pooled heavy chains from LOU rats to define the structural variability in the amino terminal region of the rat heavy chain. Characteristic VHIII sequences were found in both the myeloma proteins and the heavy chains from the pool. The data confirm previous conclusions concerning the rat VHIII subgroup that had been derived from studies of pooled heavy chains from Sprague-Dawley rats. In particular phylogenetically associated residues, identical to those previously determined in the Sprague-Dawley pool, were found in the LOU/C/Wsl rat myeloma proteins. There were two unexpected findings: 1) hypervariability at position 16 of the rat VHIII myelomas as contrasted with more than 90% glycine in the pool, and 2) a striking homology of one rat myeloma heavy chain with the variable region of the MOPC 315 mouse alpha-chain. The findings show that the rat myeloma system provides useful proteins for sequence analysis but indicate that some sequence pattern differences can be detected between the myeloma proteins and pooled immunoglobulins from this species.

Amino Acid Sequence↗
PubMed1975

Binding parameters of the interaction between rat IgE and rat mast cell receptors.

Rat monoclonal IgE was purified by a combination of gel filtration and isoelectric focusing. The binding parameters of the IgE-target cell interaction were studied. The target cells used were normal rat peritoneal mast cells (RMC) and neoplastic rat basophilic leukocytes (RBL). BINDING assays were performed by adding different amounts of IgE to a constant cell number. A Scatchard analysis of the data indicated that both cell types have a similar affinity for rat IgE; the equilibrium constant was in the order of 10-9 M-minus 1. However, RBL have a higher number of receptor sites per cell--approximately 6 times 10-5 versus 3 times 10-5 for normal RMC. Since RMC have more than double the surface area of RBL, the data indicate a much higher receptor density on RBL.

Animals↗